ID A0A0V1L4J7_9BILA Unreviewed; 907 AA.
AC A0A0V1L4J7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 28-JUN-2023, entry version 26.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
DE Flags: Fragment;
GN Name=TOP3A {ECO:0000313|EMBL:KRZ54327.1};
GN ORFNames=T02_9895 {ECO:0000313|EMBL:KRZ54327.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ54327.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ54327.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ54327.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Introduces a single-strand break via transesterification at a
CC target site in duplex DNA. Releases the supercoiling and torsional
CC tension of DNA introduced during the DNA replication and transcription
CC by transiently cleaving and rejoining one strand of the DNA duplex. The
CC scissile phosphodiester is attacked by the catalytic tyrosine of the
CC enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme
CC intermediate and the expulsion of a 3'-OH DNA strand.
CC {ECO:0000256|RuleBase:RU362092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000213,
CC ECO:0000256|RuleBase:RU362092};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|RuleBase:RU362092}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ54327.1}.
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DR EMBL; JYDW01000140; KRZ54327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1L4J7; -.
DR STRING; 6335.A0A0V1L4J7; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 1.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR023406; Topo_IA_AS.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013825; Topo_IA_cen_sub2.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR013498; Topo_IA_Znf.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF01396; zf-C4_Topoisom; 1.
DR Pfam; PF06839; zf-GRF; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
DR PROSITE; PS51999; ZF_GRF; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362092};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 40..187
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 799..841
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ54327.1"
FT NON_TER 907
FT /evidence="ECO:0000313|EMBL:KRZ54327.1"
SQ SEQUENCE 907 AA; 102327 MW; 78D6A55306A376BA CRC64;
LLFSKAAKNN SRNSLVFLKC SGKYFLQFDV VCVGLAIMRR VLNVAEKNDA SRTIAQILSR
GQMNRREGFS KFNKIYEFNC TVFGELCRMV FTSVSGHLLN LDFDSIYRNW QSVPVEELFT
APVLKRCSPD MQPVLRTLQA EVRMVDLLVI WTDCDREGEN IGFEVIGVCL EVKPSLVVKR
AVFSELTSQA ITRALASLTE PNALLSDAVD CRQEMDLRTG AAFTRFQTLR LRDTFKRQLG
DKLISYGSCQ FPTLGLVVDR YKQNQAFICE TFWKLVAKHE TVEFHWRRGR LFDRHACATL
LQLCLESPVA VVRAVRSRKR TRKRPVALDT VSLEKMACKR LGMTAKEAMA VAEKLYTQGY
ISYPRTETNF FPKEIDLVSL VKQHVNDSQW GTFANRVLSQ GVQPRQGNKT DNAHPPIHPI
RHVDLEQFQH QQHRRLYEFV VRHFLACISA DAQGLQTTVE IEVADEQFSA SGLIVTERNY
LEVYHPYENW SEKQLDVAYA VGDRFDVQVE MVTGETKPPN LLTEADLISL MEKFGIGTDA
THAEHIETIQ KRLYVGLTAD KRLLPGFLGL GLVDGYDAIG CQLAKPDLRA DFETELRRIA
NGSRSKQDVL GEYKTKYWHV FMQVTAMAER LDQALSAYFD SGTGPSTVAV SGQSDNNYSA
RRQEQQQLDN VCTRCLSCGN SMRLKQTRNG IYFVGCENYP SCKEAIWLDQ RERIQFASVL
ADRCDWCTLR QTRLIELKLA PNPLTTSRIC VTCPASNKLQ TRQLPPNPPP PAFVQLDGAR
VSLPAPGPEP SAQENQPICQ CGLPSKLFTV RKEGPNKGRT FYSCSKIGHG KCNFFVWADV
GPLPLSRSTM VQSQSNTFGQ YFPQSTRQTC HNASRGSQAG SGIKAVRKCG LCRQPGHNVK
NCPEKFT
//
